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Entry: G0A2C8_METMM
LinkDB: G0A2C8_METMM
Original site: G0A2C8_METMM 
ID   G0A2C8_METMM            Unreviewed;       254 AA.
AC   G0A2C8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=ATP synthase subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
DE   AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
DE   AltName: Full=ATPase subunit I {ECO:0000256|HAMAP-Rule:MF_01398};
DE   AltName: Full=F-type ATPase subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
DE            Short=F-ATPase subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
GN   Name=atpF {ECO:0000256|HAMAP-Rule:MF_01398};
GN   OrderedLocusNames=Metme_0496 {ECO:0000313|EMBL:AEF98940.1};
OS   Methylomonas methanica (strain MC09).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomonas.
OX   NCBI_TaxID=857087 {ECO:0000313|EMBL:AEF98940.1, ECO:0000313|Proteomes:UP000008888};
RN   [1] {ECO:0000313|EMBL:AEF98940.1, ECO:0000313|Proteomes:UP000008888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC09 {ECO:0000313|EMBL:AEF98940.1,
RC   ECO:0000313|Proteomes:UP000008888};
RX   PubMed=22123758; DOI=10.1128/JB.06267-11;
RA   Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M.G.,
RA   Jetten M.S., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H.,
RA   Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.F., Goodwin L.,
RA   Han C., Hauser L., Land M.L., Lapidus A., Lucas S., Pitluck S., Woyke T.,
RA   Stein L., Murrell J.C.;
RT   "Complete Genome Sequence of the Aerobic Marine Methanotroph Methylomonas
RT   methanica MC09.";
RL   J. Bacteriol. 193:7001-7002(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MC09;
RA   Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M.,
RA   Jetten M., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H.,
RA   Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.-F., Goodwin L.,
RA   Han C., Hauser L., Land M., Lapidus A., Lucas S., Pitluck S., Woyke T.,
RA   Stein L.Y., Murrell C.;
RT   "Complete genome sequence of the aerobic marine methanotroph Methylomonas
RT   methanica MC09.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000008888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC09 {ECO:0000313|Proteomes:UP000008888};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Stein L., Woyke T.;
RT   "Complete sequence of Methylomonas methanica MC09.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC       peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged
CC       and duplicated form of b found in plants and photosynthetic bacteria.
CC       {ECO:0000256|ARBA:ARBA00025614}.
CC   -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC       of a proton or sodium gradient. F-type ATPases consist of two
CC       structural domains, F(1) containing the extramembraneous catalytic core
CC       and F(0) containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC       in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC       the central stalk subunits to proton translocation.
CC       {ECO:0000256|ARBA:ARBA00025198, ECO:0000256|HAMAP-Rule:MF_01398}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC       - and F(0) - the membrane proton channel. F(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main
CC       subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an
CC       alternating ring which encloses part of the gamma chain. F(1) is
CC       attached to F(0) by a central stalk formed by the gamma and epsilon
CC       chains, while a peripheral stalk is formed by the delta and b chains.
CC       {ECO:0000256|HAMAP-Rule:MF_01398}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01398}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01398}. Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the ATPase B chain family.
CC       {ECO:0000256|ARBA:ARBA00005513, ECO:0000256|HAMAP-Rule:MF_01398}.
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DR   EMBL; CP002738; AEF98940.1; -; Genomic_DNA.
DR   RefSeq; WP_013817212.1; NC_015572.1.
DR   AlphaFoldDB; G0A2C8; -.
DR   STRING; 857087.Metme_0496; -.
DR   KEGG; mmt:Metme_0496; -.
DR   eggNOG; COG0711; Bacteria.
DR   HOGENOM; CLU_070737_0_0_6; -.
DR   OrthoDB; 466272at2; -.
DR   Proteomes; UP000008888; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   CDD; cd06503; ATP-synt_Fo_b; 1.
DR   HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR   InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR   InterPro; IPR005864; ATP_synth_F0_bsu_bac.
DR   NCBIfam; TIGR01144; ATP_synt_b; 1.
DR   PANTHER; PTHR33445:SF2; ATP SYNTHASE SUBUNIT B; 1.
DR   PANTHER; PTHR33445; ATP SYNTHASE SUBUNIT B', CHLOROPLASTIC; 1.
DR   Pfam; PF00430; ATP-synt_B; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW   Rule:MF_01398}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01398};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01398};
KW   CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|HAMAP-Rule:MF_01398};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW   Rule:MF_01398};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_01398};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01398};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008888};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01398};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01398};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01398}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01398"
FT   COILED          38..72
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   254 AA;  29172 MW;  79FE585118918147 CRC64;
     MQIDWLTVAA QWINFLILMW LLRRYLYQPI IQAMDKRQQT LAASAQAAEQ KMRQAEQQAE
     LYRNKLAELE AHGAALMTAA RQAADNEREK LVGQARTEFE TLAQQWRRDL EREKAAFQHQ
     LRNELGQLIT ATARKAVIDL TGRELEQALF DNFLSRLNAL TAEDKQLLSE SGRENTVLAS
     SCELGEASRI RFTDALNRTL PSPINIRFET LPDSRLGLLL TTPAYTLEWR VERYFADLQT
     ELDSVLNAQQ HQPC
//
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